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identifier: 1772912
description:
epitope description:P1390, Q1391, R1392, S1394, R1395, N1396, F1397, V1398, R1399, N1421, K1423, Q1424, L1427
antigen name:von Willebrand factor
host organism:Mus musculus
antibody name:NMC-4
aggregation:
instance of dataset
availability:
available
primaryPublications: 9501911
authorizations:
registration not required
accessURL: http://www.iedb.org/reference/496
landingPage: http://www.iedb.org/assay/1772912
type:
Literature
publicationVenue:
Nat Struct Biol
dates:
1998
study type: b cell assays
subject species: Homo sapiens
fullName:
R Celikel
K I Varughese
Madhusudan
A Yoshioka
J Ware
Z M Ruggeri
method:
ELISA
name:
Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab.
description:
Epitope residues were calculated from the structure [PDB: 1OAK] as the antigen residues interacting with the antibody fragment at atomic distance of 4 Å
. Mapping of residue numbers between PDB and GenBank was done as provided in PDB.
Epitope specific Fab NMC-4 bound to the vWF A1 domain. A1 domain mutants with Arg632 or Arg636 replaced by Ala do not bind Fab NMC-4, confirming their importance as antibody contact residues. The mutations did not affect A1 domain binding to GP Ibalpha under blood flow conditions.

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